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{{PBB|geneid=9313}}
{{Infobox_gene}}
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'''Matrix metalloproteinase-20''' (MMP-20) also known as '''enamel metalloproteinase''' or '''enamelysin''' is an [[enzyme]] that in humans is encoded by the ''MMP20'' [[gene]].<ref name="pmid9398237">{{cite journal |vauthors=Llano E, Pendas AM, Knauper V, Sorsa T, Salo T, Salido E, Murphy G, Simmer JP, Bartlett JD, Lopez-Otin C | title = Identification and structural and functional characterization of human enamelysin (MMP-20) | journal = Biochemistry | volume = 36 | issue = 49 | pages = 15101–15108 |date=Jan 1998 | pmid = 9398237 | pmc =  | doi = 10.1021/bi972120y }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: MMP20 matrix metallopeptidase 20 (enamelysin)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9313| accessdate = }}</ref>


== Function ==


'''Matrix metallopeptidase 20 (enamelysin)''', also known as '''MMP20''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MMP20 matrix metallopeptidase 20 (enamelysin)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9313| accessdate = }}</ref>
Proteins of the matrix metalloproteinase ([[matrix metalloproteinase|MMP]]) family are involved in the breakdown of [[extracellular matrix]] in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular [[proteinase]]s.


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
MMP-20, also known as enamelysin, appears to be the only MMP that is tooth-specific and it is expressed by cells of different developmental origin (i.e. epithelial [[ameloblast]]s and mesenchymal [[odontoblast]]s).
{{PBB_Summary
| section_title =
| summary_text = Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The protein encoded by this gene degrades amelogenin, the major protein component of dental enamel matrix, and so the protein is thought to play a role in tooth enamel formation. A mutation in this gene, which alters the normal splice pattern and results in premature termination of the encoded protein, has been associated with [[Amelogenesis imperfecta]]. This gene is part of a cluster of MMP genes that localizes to chromosome 11q22.3.<ref name="entrez">{{cite web | title = Entrez Gene: MMP20 matrix metallopeptidase 20 (enamelysin)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9313| accessdate = }}</ref>
}}


==References==
== Clinical significance ==
{{reflist|2}}
 
==Further reading==
The human MMP-20 gene contains 10 exons and is part of a cluster of matrix metalloproteinase genes that localize to human chromosome 11q22.3.<ref name="entrez" /> A mutation in this gene, which alters the normal splice pattern and results in premature termination of the encoded protein, has been associated with [[amelogenesis imperfecta]]. Enamel in the absence of MMP-20 is hypoplastic (thin), contains less mineral (only one-third as much total mineral as wild type), and contains more protein and water. In general, MMP-20 functions in enamel are to cleave enamel matrix proteins at specific cleavage sites.<ref name="pmid22652761">{{cite journal | author = Moradian-Oldak J | title = Protein-mediated enamel mineralization | journal = Front. Biosci. | volume = 17 | issue = | pages = 1996–2023 | year = 2012 | pmid = 22652761 | pmc = 3442115 | doi = 10.2741/4034}}</ref>
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
*{{cite journal  |vauthors=Nagase H, Woessner JF |title=Matrix metalloproteinases |journal=J. Biol. Chem. |volume=274 |issue= 31 |pages= 21491–21494 |year= 1999 |pmid= 10419448 |doi=10.1074/jbc.274.31.21491 }}
| citations =
*{{cite journal  |vauthors=Bartlett JD, Simmer JP |title=Proteinases in developing dental enamel |journal=Crit. Rev. Oral Biol. Med. |volume=10 |issue= 4 |pages= 425–441 |year= 2000 |pmid= 10634581 |doi=10.1177/10454411990100040101 }}
*{{cite journal  | author=Nagase H, Woessner JF |title=Matrix metalloproteinases. |journal=J. Biol. Chem. |volume=274 |issue= 31 |pages= 21491–4 |year= 1999 |pmid= 10419448 |doi=  }}
*{{cite journal  | author=Pendás AM |title=Fine physical mapping of the human matrix metalloproteinase genes clustered on chromosome 11q22.3 |journal=Genomics |volume=37 |issue= 2 |pages= 266–269 |year= 1997 |pmid= 8921407 |doi=10.1006/geno.1996.0557 |name-list-format=vanc| author2=Santamaría I  | author3=Alvarez MV  | display-authors=3  | last4=Pritchard  | first4=M  | last5=López-Otín  | first5=C  }}
*{{cite journal  | author=Bartlett JD, Simmer JP |title=Proteinases in developing dental enamel. |journal=Crit. Rev. Oral Biol. Med. |volume=10 |issue= 4 |pages= 425–41 |year= 2000 |pmid= 10634581 |doi=  }}
*{{cite journal  | author=Stracke JO |title=Matrix metalloproteinases 19 and 20 cleave aggrecan and cartilage oligomeric matrix protein (COMP) |journal=FEBS Lett. |volume=478 |issue= 1–2 |pages= 52–56 |year= 2000 |pmid= 10922468 |doi=10.1016/S0014-5793(00)01819-6  |name-list-format=vanc| author2=Fosang AJ  | author3=Last K  | display-authors=3  | last4=Mercuri  | first4=FA  | last5=Pendás  | first5=AM  | last6=Llano  | first6=E  | last7=Perris  | first7=R  | last8=Di Cesare  | first8=PE  | last9=Murphy  | first9=G }}
*{{cite journal  | author=Pendás AM, Santamaría I, Alvarez MV, ''et al.'' |title=Fine physical mapping of the human matrix metalloproteinase genes clustered on chromosome 11q22.3. |journal=Genomics |volume=37 |issue= 2 |pages= 266–8 |year= 1997 |pmid= 8921407 |doi= }}
*{{cite journal  |vauthors=Terp GE, Christensen IT, Jørgensen FS |title=Structural differences of matrix metalloproteinases. Homology modeling and energy minimization of enzyme-substrate complexes |journal=J. Biomol. Struct. Dyn. |volume=17 |issue= 6 |pages= 933–46 |year= 2000 |pmid= 10949161 |doi=10.1080/07391102.2000.10506582 }}
*{{cite journal | author=Llano E, Pendás AM, Knäuper V, ''et al.'' |title=Identification and structural and functional characterization of human enamelysin (MMP-20). |journal=Biochemistry |volume=36 |issue= 49 |pages= 15101–8 |year= 1998 |pmid= 9398237 |doi= 10.1021/bi972120y }}
*{{cite journal  | author=Väänänen A |title=Expression and regulation of MMP-20 in human tongue carcinoma cells |journal=J. Dent. Res. |volume=80 |issue= 10 |pages= 1884–1889 |year= 2001 |pmid= 11706946 |doi=10.1177/00220345010800100501  |name-list-format=vanc| author2=Srinivas R  | author3=Parikka M  | display-authors=3  | last4=Palosaari  | first4=H.  | last5=Bartlett  | first5=J.D.  | last6=Iwata  | first6=K.  | last7=Grenman  | first7=R.  | last8=Stenman  | first8=U.-H.  | last9=Sorsa  | first9=T. }}
*{{cite journal  | author=Stracke JO, Fosang AJ, Last K, ''et al.'' |title=Matrix metalloproteinases 19 and 20 cleave aggrecan and cartilage oligomeric matrix protein (COMP). |journal=FEBS Lett. |volume=478 |issue= 1-2 |pages= 52–6 |year= 2000 |pmid= 10922468 |doi=  }}
*{{cite journal  | author=Väänänen A |title=Expression of collagen XVIII and MMP-20 in developing teeth and odontogenic tumors |journal=Matrix Biol. |volume=23 |issue= 3 |pages= 153–161 |year= 2005 |pmid= 15296943 |doi= 10.1016/j.matbio.2004.04.003 |name-list-format=vanc| author2=Tjäderhane L  | author3=Eklund L  | display-authors=3  | last4=Heljasvaara  | first4=R  | last5=Pihlajaniemi  | first5=T  | last6=Herva  | first6=R  | last7=Ding  | first7=Y  | last8=Bartlett  | first8=JD  | last9=Salo  | first9=T }}
*{{cite journal  | author=Terp GE, Christensen IT, Jørgensen FS |title=Structural differences of matrix metalloproteinases. Homology modeling and energy minimization of enzyme-substrate complexes. |journal=J. Biomol. Struct. Dyn. |volume=17 |issue= 6 |pages= 933–46 |year= 2000 |pmid= 10949161 |doi=  }}
*{{cite journal  | author=Kim JW |title=MMP-20 mutation in autosomal recessive pigmented hypomaturation amelogenesis imperfecta |journal=J. Med. Genet. |volume=42 |issue= 3 |pages= 271–275 |year= 2006 |pmid= 15744043 |doi= 10.1136/jmg.2004.024505 | pmc=1736010  |name-list-format=vanc| author2=Simmer JP  | author3=Hart TC  | display-authors=3  | last4=Hart  | first4=PS  | last5=Ramaswami  | first5=MD  | last6=Bartlett  | first6=JD  | last7=Hu  | first7=JC }}
*{{cite journal  | author=Väänänen A, Srinivas R, Parikka M, ''et al.'' |title=Expression and regulation of MMP-20 in human tongue carcinoma cells. |journal=J. Dent. Res. |volume=80 |issue= 10 |pages= 1884–9 |year= 2001 |pmid= 11706946 |doi=  }}
*{{cite journal  | author=Väänänen A, Tjäderhane L, Eklund L, ''et al.'' |title=Expression of collagen XVIII and MMP-20 in developing teeth and odontogenic tumors. |journal=Matrix Biol. |volume=23 |issue= 3 |pages= 153–61 |year= 2005 |pmid= 15296943 |doi= 10.1016/j.matbio.2004.04.003 }}
*{{cite journal  | author=Kim JW, Simmer JP, Hart TC, ''et al.'' |title=MMP-20 mutation in autosomal recessive pigmented hypomaturation amelogenesis imperfecta. |journal=J. Med. Genet. |volume=42 |issue= 3 |pages= 271–5 |year= 2006 |pmid= 15744043 |doi= 10.1136/jmg.2004.024505 }}
}}
{{refend}}
{{refend}}


==External links==
* The [[MEROPS]] online database for peptidases and their inhibitors: [http://merops.sanger.ac.uk/cgi-bin/merops.cgi?id=M10.019 M10.019]
{{Metalloendopeptidases}}
{{Enzymes}}
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[[Category:Matrix metalloproteinases]]
[[Category:EC 3.4.24]]


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Latest revision as of 04:23, 27 October 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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PubMed searchn/an/a
Wikidata
View/Edit Human

Matrix metalloproteinase-20 (MMP-20) also known as enamel metalloproteinase or enamelysin is an enzyme that in humans is encoded by the MMP20 gene.[1][2]

Function

Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases.

MMP-20, also known as enamelysin, appears to be the only MMP that is tooth-specific and it is expressed by cells of different developmental origin (i.e. epithelial ameloblasts and mesenchymal odontoblasts).

Clinical significance

The human MMP-20 gene contains 10 exons and is part of a cluster of matrix metalloproteinase genes that localize to human chromosome 11q22.3.[2] A mutation in this gene, which alters the normal splice pattern and results in premature termination of the encoded protein, has been associated with amelogenesis imperfecta. Enamel in the absence of MMP-20 is hypoplastic (thin), contains less mineral (only one-third as much total mineral as wild type), and contains more protein and water. In general, MMP-20 functions in enamel are to cleave enamel matrix proteins at specific cleavage sites.[3]

References

  1. ↑ Llano E, Pendas AM, Knauper V, Sorsa T, Salo T, Salido E, Murphy G, Simmer JP, Bartlett JD, Lopez-Otin C (Jan 1998). "Identification and structural and functional characterization of human enamelysin (MMP-20)". Biochemistry. 36 (49): 15101–15108. doi:10.1021/bi972120y. PMID 9398237.
  2. ↑ 2.0 2.1 "Entrez Gene: MMP20 matrix metallopeptidase 20 (enamelysin)".
  3. ↑ Moradian-Oldak J (2012). "Protein-mediated enamel mineralization". Front. Biosci. 17: 1996–2023. doi:10.2741/4034. PMC 3442115. PMID 22652761.

Further reading

External links

  • The MEROPS online database for peptidases and their inhibitors: M10.019


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